Difference between revisions of "Phosphatase Subfamily DSP23"

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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
  
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summary...
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DSP23 is a nuclear phosphatase found in metazoan but lost in ecdysozoan.
  
 
=== Evolution ===
 
=== Evolution ===
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=== Function ===
 
=== Function ===
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Laforin is a glucan phosphatase <cite>Worby06, Gentry07</cite>.
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Human DUSP23 dephosphorylates Ser322 on Glial cells missing homolog 1 (GCM1), which is a transcription factor essential for placental development. The dephosphorylation promotes GCM1 acetylation <cite>Lin11</cite>.  
  
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laforin is also a phosphatase of muscle glycogen synthase (GS1) in polyglucosan bodies (PBs).
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DSP23 is also called VHZ for its similarity with VHR phosphatase. Different from MAP kinases phosphatases which negatively regulate MAP kinases such as JNK and p38, DSP23 has been reported to enhance activation of JNK and p38 <cite>Takagaki04</cite>. Human DSP23 locates at centrosome in [http://en.wikipedia.org/wiki/MCF-7 MCF-7] cells and is proposed to be involved in cell growth and human primary cancers. <cite>Tang10</cite>.  
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In [http://en.wikipedia.org/wiki/Lafora_disease Lafora disease] (LD), the deficiency of either laforin or E3 ligase malin causes massive accumulation of less-branched glycogen inclusions, known as [http://en.wikipedia.org/wiki/Lafora_disease#Lafora_bodies Lafora bodies], also called polyglucosan bodies (PBs), in several types of cells including neurons. Once GS1-synthesized polyglucosan accumulates into PBs, laforin recruits malin to the PBs where laforin dephosphorylates, and malin degrades the GS1 in concert with GPBB and AGL1, resulting in a breakdown of polyglucosan <cite>Liu14</cite>. Laforin also dephosphorylates Ser 9 of Glycogen synthase kinase 3 <cite>Lohi05</cite>.
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Laforin also as an adaptor protein involved in several physiological pathways <cite>Gentry13</cite>. For instance, the complex of laforin and malin modules protein phosphatase 1 regulatory subunit PPP1R3D via ubiquitination <cite>Rubio-Villena13</cite>. See <cite>Gentry13</cite> for details.
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=== Links ===
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[http://phosphatome.net/3.0/database/gene/uid/HsapP023 Human DUSP23 page] in Phosphatome.Net database.
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=== References ===
 
=== References ===
 
<biblio>
 
<biblio>
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#Alonso04 pmid=15201283
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#Lin11 pmid=20855292
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#Takagaki04 pmid=15281913
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#Tang10 pmid=20509867
 
</biblio>
 
</biblio>

Revision as of 20:53, 2 March 2015

Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily DSP23

DSP23 is a nuclear phosphatase found in metazoan but lost in ecdysozoan.

Evolution

DSP23 is found in metazoan but lost in nematodes and most arthropods (unpublished data from gOrtholog) has a single member in human, DUSP23.

Domain

DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family [1].

Function

Human DUSP23 dephosphorylates Ser322 on Glial cells missing homolog 1 (GCM1), which is a transcription factor essential for placental development. The dephosphorylation promotes GCM1 acetylation [2].

DSP23 is also called VHZ for its similarity with VHR phosphatase. Different from MAP kinases phosphatases which negatively regulate MAP kinases such as JNK and p38, DSP23 has been reported to enhance activation of JNK and p38 [3]. Human DSP23 locates at centrosome in MCF-7 cells and is proposed to be involved in cell growth and human primary cancers. [4].

References

Error fetching PMID 15201283:
Error fetching PMID 20855292:
Error fetching PMID 15281913:
Error fetching PMID 20509867:
  1. Error fetching PMID 15201283: [Alonso04]
  2. Error fetching PMID 20855292: [Lin11]
  3. Error fetching PMID 15281913: [Takagaki04]
  4. Error fetching PMID 20509867: [Tang10]
All Medline abstracts: PubMed | HubMed
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